Pulsed Electric Field on Dairy and Plant Proteins

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1		Ahmed Taha	--	2336	2022-06-06 15:53:37	\|
2	update references and layout	Amina Yu	-16 word(s)	2320	2022-06-07 03:07:17	\|

This entry is adapted from the peer-reviewed paper 10.3390/foods11111556

Dairy and plant-based proteins are widely utilized in various food applications. Several techniques have been employed to improve the techno-functional properties of these proteins. Among them, pulsed electric field (PEF) technology has recently attracted considerable attention as a green technology to enhance the functional properties of food proteins. The PEF treatment conditions markedly affect the treatment results with respect to proteins’ structure and techno-functional properties.

pulsed electric field milk proteins plant proteins

1. Effects of Pulsed Electric Field (PEF) on the Structure of Dairy and Plant Proteins

Caseins consist of four major subunits, including αs1, αs2, β, and kappa caseins. Whey proteins have several subunits, including β-lactoglobulin (β-LG), α-lactalbumin (α-LA), bovine serum albumin (BSA), lactoferrin, and traces of some other components, such as immunoglobulins and glycomacropeptide ^[1]^[2]. In general, upon thermal treatment of milk proteins, proteins unfold because of covalent bonds breaking, and sulfhydryl (-SH) groups are exposed to the protein surface; then, aggregates are produced due to the formation of disulfide bonds.

Moreover, as free thiol groups are not available in α-LA, it is less sensitive to thermal treatment than β-LG ^[3]. It has been shown that PEF can change the structure of dairy proteins, especially at higher electric strengths at a wide range of temperatures ^[4]. The energy generated by PEF devices could expose amino acid and/or free-SH groups to the protein molecules’ surface. Moreover, non-covalent interactions, such as hydrophobic and hydrogen bonds, may be disrupted ^[3]. Furthermore, it was found that PEF can change the charge density around amino acids (at the -COOH and -NH3⁺ moieties), influencing the catalytic activity of peptides ^[5]. Whey proteins have recently attracted attention due to their nutritional benefits and industrial applications.

The available results about PEF effects on the structure of whey proteins are somehow contradictory. Sui et al. ^[6] investigated the effects of PEF and heat treatments (30–35 kV/cm, 19.2–211 µs, 30–75 °C) on the physicochemical and functional properties of whey protein isolates (WPI). They concluded that PEF treatment did not influence protein unfolding, surface hydrophobicity, of free-SH group content ^[6]. Using a different treatment chamber with a different distance between electrodes, Xiang et al. ^[7] found that PEF increased the surface hydrophobicity and the extrinsic fluorescence intensity of WPI. Similarly, Perez et al. ^[8] noticed that PEF treatment (12.5 kV/cm) with up to 10 pulses changed the native structure of β-LG and induced protein aggregation. The differences between the results may occur due to the use of various experimental conditions, such as treatment chamber, electric field intensity, frequency, and temperature ^[9]. Bovine lactoferrin was treated using PEF at different temperatures (30–70 °C) and compared with non-PEF-treated samples at the same temperatures ^[10]. The results showed that the lactoferrin concentration was not changed by the PEF treatment (35 kV/cm, 19.2 µs, 30–70 °C). Moreover, SDS-PAGE results indicated no significant difference in the gel profile of PEF and non-PEF-treated lactoferrin. The surface hydrophobicity increased with increased temperature. There were no significant differences in surface hydrophobicity values between PEF- and non-PEF-treated lactoferrin ^[10]. Bekard et al. ^[11] studied the effects of a low-intensity electric field on the conformational state of BSA using circular dichroism (CD) spectroscopy. They concluded that a low-intensity electric field (500 V/m, 3 h at 22.7–24.2 °C) changed the tertiary structure of BSA, probably due to perturbation in the hydrogen bonds that stabilized the native structure of BSA ^[11]. Sharma et al. ^[12] preheated milk samples to 55 °C for 24 s and then applied PEF at 20–26 kV/cm for 34 µs. The results indicated that the surface hydrophobicity of milk proteins considerably increased with increased electric field intensity. Thermal treatment at 30–55 °C can dissociate β-LG dimers into monomers ^[13]. Thermal pre-treatment associated with PEF might facilitate the dissociation of β-LG dimers of milk samples and expose hydrophobic groups and free-SH groups to the protein molecules’ surfaces ^[12]. Rodrigues et al. ^[14] compared conventional heat treatment with moderate electric field (MEF, 20–80 V/cm) heating at 50–90 °C. They found that with 70 °C and 80 °C treatments, moderate electric field treatment exhibited higher content of α-helix and random coils and lower content of β-sheet compared to conventional heat treatment at the same temperature. These structural changes probably occurred due to the effects of both heat treatment and electric field on the conformational state of β-LG.

Caseins are the major proteins in milk (80% of total milk protein) and one of the main protein sources in human nutrition. The effects of PEF on the structure of caseins are scarce. Subaşı et al. ^[15] studied the impact of MEF (230 V/cm) on the structural changes of sodium caseinate compared to sunflower protein. FTIR data revealed that MEF can change the secondary structure of sodium caseinate and unfold the protein molecules. This is probably because MEF treatment can polarize the surface of protein molecules, facilitating the exposure of hydrophobic regions to the surface of protein molecules ^[8]^[15].

The mechanism of PEF effects on milk protein structures can be proposed based on the available information. Generally, PEF treatments at low electric field intensities have no apparent effects on the structure of milk proteins. In contrast, PEF treatments at high electric field intensities can considerably change protein structures, especially in whey proteins.

Some polar groups of milk proteins absorb energy and produce free radicals when exposed to intensive electric fields. These free radicals can disrupt the several interactions among protein molecules, including disulfide and hydrogen bonds, as well as hydrophobic, electrostatic, and Van der Waals interactions. Moreover, the electric field can affect the strong dipole moment of the polypeptide chains, increasing the dielectric constant of proteins. These changes may facilitate the unfolding of protein molecules and the exposure of hydrophobic and -SH groups to the surface of protein molecules. Increasing the duration of PEF treatment could result in the formation of aggregates, as covalent and hydrophobic interaction may occur to crosslink unfolded protein molecules ^[3]^[8]^[16]. It is worth mentioning that an increase in temperature during PEF treatment could facilitate the denaturation of protein molecules. Thus, further effects of PEF on protein structures under controlled temperatures is recommended.

PEF treatment changed the structures of plant proteins. The secondary structure of soy protein isolate (SPI) changed after PEF treatment at 30–50 kV/cm. PEF caused denaturation and aggregation to SPI, probably due to the formation of hydrophobic interactions and S–S bonds ^[17]^[18]. Exposure of sunflower protein to moderate electric field strength (150 V for 20 s at a temperature < 45 °C) resulted in secondary and tertiary structural changes. PEF treatment broke the hydrophobic bonds and facilitated the crosslinking of amino acid side chains ^[15]. Similar results were also reported with pea and canola proteins ^[19]^[20]. Generally, PEF treatment is able to alter the structure of plant proteins. These changes could also affect the techno-functional properties of such proteins.

2. Effects of PEF on the Techno-Functional Properties of Dairy and Plant Proteins

The functionality of milk proteins is determined by physicochemical properties that affect the behavior of proteins during their utilization in food systems ^[21]. The modifications of protein structures can alter their functional properties ^[22]. Techno-functional properties, including solubility, gelling, emulsifying, and foaming properties, are of considerable interest in the food industry ^[23]. Therefore, it will discuss the effects of electric field treatment on the techno-functional properties of milk proteins.

2.1. Protein Solubility

Protein solubility is commonly determined by measuring the concentration of soluble proteins after the centrifugation of protein samples and relating it to the total protein concentration before centrifugation ^[24]. Protein solubility is influenced by several intrinsic factors, such as amino acid composition, protein molecular weight, the content of hydrophilic and hydrophobic groups on proteins molecules’ surfaces, and the content of hydrogen bonds ^[25]^[26]. Several extrinsic factors can also affect the protein solubility, including temperature, ionic strength, pH, and the presence of solvents ^[27]. Protein solubility is important for several protein applications, such as emulsions and foams. Therefore, it is recommended to use highly soluble proteins to form well-dispersed colloidal systems ^[28]. The effects of electric field treatments on the solubility of several proteins were investigated. There was a decrease in the solubility of pea (from 23.2 to 17.2%), rice (from 16.4 to 9.2%), and gluten (from 25 to 22.4%) concentrates after treatment with moderate electric field strength (1.65 kV/cm, square pulse system) ^[29]. Similarly, the content of soluble egg white proteins decreased (7.84%) after PEF treatment using a PEF system with square-wave pulses (at 25 kV/cm) ^[30]. The authors also observed that the average particle size of egg white proteins increased (36.9%) after PEF treatment. PEF unfolded protein molecules and formed insoluble protein molecules. Moreover, intermolecular interactions, such as S-S bonds could occur, resulting in reduced protein solubility. However, with soy protein isolates, Li et al. ^[17] found that PEF treatment of up to 30 kV/cm using a PEF system with bipolar waveforms improved solubility, whereas PEF at strengths higher than 30 kV/cm resulted in a slight decrease in protein solubility. Additionally, PEF treatment (35 kV/cm for 8 μs) increased the solubility (50.07%) of canola protein compared to that of control samples (43.25%) ^[19]. Therefore, it was concluded that different waveforms and protein types can affect protein solubility differently. However, there is a lack of available knowledge about factors behind the desired solubility of milk proteins after PEF treatment, probably due to the confirmed higher solubility of milk proteins.

2.2. Gelling Properties

The gelling properties of proteins are closely associated with the content of -SH groups and disulfide bonds. In the dairy industry, the gelation of milk proteins is an essential factor influencing the quality of many dairy products, including cheese, yogurt, and dairy-based desserts ^[31]. Perez et al. ^[8] found that PEF improved the gelling rate of β-lactoglobulin (at 72 °C) when samples were exposed to fewer than six pulses. Yu et al. ^[32] studied the effects of PEF (20 and 30 kV/cm) at different outlet temperatures on the rennet coagulation characteristics of raw milk. They found that PEF (at 20 °C)-treated milk had higher curd firmness than pasteurized milk samples. Moreover, PEF-treated milk samples had a lower rennet coagulation time (RCT) than pasteurized milk samples. It is known that lower RCT values result in better gelling properties ^[32]. Jin et al. ^[33] concluded that the gelling properties of WPI increased when treated at 35 kV/cm but decreased after PEF treatment at 45 kV/cm. During PEF treatment, the unfolding of milk proteins and the exposure of -SH groups, followed by the formation of S-S bonds, could be the reason behind the improved gelling properties of milk. Another reason for the improved gelling properties reported in these could be the polarization of protein molecules during treatment. Polarized molecules can attract each other through electrostatic forces ^[8]. However, Sui et al. ^[10] found that PEF (30 kV/cm)-treated WPI showed lower gel strength than untreated samples; increasing the PEF duration decreased the gel strength of WPI samples. Rodrigues et al. ^[34] concluded that conventional heat-treated WPI samples had higher gel strength than those subjected to moderate electric field treatment (15–22 V/cm). At pH 7, electrostatic repulsion among protein molecules may reduce the size of protein aggregates ^[35]. Moreover, applying an electric field could destroy some of the non-covalent bonds between proteins ^[34]. The water-holding capacity of PEF-treated canola protein increased at lower electric field strength (25 kV/cm) and decreased at higher electric field strength (35 kV/cm) ^[19]. For pea protein isolate, lower electric field treatment resulted in cohesive, more elastic, and weaker gels with higher water-holding capacity ^[20]. The inconsistency of gelling properties reported in different ones could be due to the use of different PEF conditions, such as voltage, the shape of the pulse wave, and the type of treatment chamber used.

2.3. Emulsifying and Foaming Properties

The stability of emulsions is vital for improving the shelf life of emulsion-based food products, such as mayonnaise, ice cream, butter, milk, and margarine. Therefore, several emulsifiers are used to reduce interfacial tension, improving the stability of emulsions ^[36]. Among them, proteins are widely used as natural emulsifiers due to their surface-active properties ^[37]^[38]. Several processing technologies, such as high-pressure treatment ^[25], ultrasound ^[36]^[39], cold plasma treatment ^[40], and microwaves ^[41], have been used to improve the emulsifying properties of proteins. On the effects of PEF on the emulsifying foaming properties of milk proteins are scarce. Sui et al. ^[6] compared the effects of heat treatment and PEF on the emulsifying properties of WPI. They observed that emulsions stabilized by PEF-treated (30 kV/cm) and heat-treated (72 °C for 15 s) samples had similar droplet sizes (~4 μm), whereas emulsions stabilized by WPI heated for 10 min had significantly larger droplet sizes (18.3 μm). Sun et al. ^[42] studied the effects of PEF treatment (15 and 30 kV/cm) on the emulsifying properties of a WPI–dextran mixture. They found that the PEF-treated mixture had a higher emulsifying activity index (EAI) than the untreated mixture ^[42]. PEF could facilitate the glycosylation reaction between WPI and dextran. The combination of protein and polysaccharides was confirmed to improve the stability of emulsions. This could be because the hydrophobic regions of proteins can be adsorbed at the surface of oil droplets, and the hydrophilic part of polysaccharides can be oriented towards the water phase, preventing the coalescence of oil droplets through steric stabilization ^[36]. Zhang et al. ^[19] found that PEF pre-treatment of canola seeds prior oil and protein extraction improved the emulsifying and foaming properties of the resulting canola proteins. PEF could improve the solubility of plant proteins and promote the exposure of their hydrophobic groups to the surface, thus improving their emulsifying and foaming properties. More are needed to understand the effects of PEF treatment on the emulsifying and foaming properties of plant and milk proteins. The changes in the protein structures induced by PEF treatment could improve the techno-functional properties of proteins. PEF could polarize and unfold protein molecules, exposing the hydrophobic groups to the surface of molecules ^[16]. Additionally, PEF can increase solubility and reduce the particle size of protein molecules at a certain electric field strength. These changes could reduce the interfacial tension at the oil/water interface, improve the emulsifying properties of food proteins, and enhance the stability of protein-stabilized emulsions ^[43]. However, there is still a lack of detailed information on the mechanism of action of PEF and its effects on protein functionality due to the limited number of studies conducted in this area. Thus, more fundamental research at the molecular scale is required to establish a clear mechanism of PEF effects on protein functionality.

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